NMD3B_RAT
ID NMD3B_RAT Reviewed; 1002 AA.
AC Q8VHN2;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Glutamate receptor ionotropic, NMDA 3B;
DE Short=GluN3B;
DE AltName: Full=N-methyl-D-aspartate receptor subtype 3B;
DE Short=NMDAR3B;
DE Short=NR3B;
DE Flags: Precursor;
GN Name=Grin3b;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=11823786; DOI=10.1038/nature715;
RA Chatterton J.E., Awobuluyi M., Premkumar L.S., Takahashi H., Talantova M.,
RA Shin Y., Cui J., Tu S., Sevarino K.K.A., Nakanishi N., Tong G.,
RA Lipton S.A., Zhang D.;
RT "Excitatory glycine receptors containing the NR3 family of NMDA receptor
RT subunits.";
RL Nature 415:793-798(2002).
RN [2]
RP SEQUENCE REVISION.
RA Chatterton J.E., Awobuluyi M., Cui J., Sevarino K.K.A., Lipton S.A.,
RA Zhang D.;
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP IDENTIFICATION, AND TISSUE SPECIFICITY.
RX PubMed=11735224; DOI=10.1006/geno.2001.6666;
RA Andersson O., Stenqvist A., Attersand A., von Euler G.;
RT "Nucleotide sequence, genomic organization, and chromosomal localization of
RT genes encoding the human NMDA receptor subunits NR3A and NR3B.";
RL Genomics 78:178-184(2001).
CC -!- FUNCTION: NMDA receptor subtype of glutamate-gated ion channels with
CC reduced single-channel conductance, low calcium permeability and low
CC voltage-dependent sensitivity to magnesium. Mediated by glycine.
CC -!- SUBUNIT: Forms heteromeric channel of a zeta subunit (GRIN1), a epsilon
CC subunit (GRIN2A, GRIN2B, GRIN2C or GRIN2D) and a third subunit (GRIN3A
CC or GRIN3B). Does not form functional homomeric channels. Found in a
CC complex containing GRIN1 and GRIN2A (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Postsynaptic cell membrane {ECO:0000250}.
CC Note=Requires the presence of GRIN1 to be targeted at the plasma
CC membrane. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in the hippocampus, the corpus callosum,
CC in the facial and trigeminal nuclei of the brainstem and the ventral
CC horn of the spinal cord. {ECO:0000269|PubMed:11735224,
CC ECO:0000269|PubMed:11823786}.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. NR3B/GRIN3B subfamily. {ECO:0000305}.
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DR EMBL; AF440691; AAL69893.2; -; mRNA.
DR RefSeq; NP_579842.2; NM_133308.2.
DR PDB; 2RCA; X-ray; 1.58 A; A/B=413-560, A/B=676-815.
DR PDB; 2RCB; X-ray; 1.62 A; A/B=413-560, A/B=676-815.
DR PDBsum; 2RCA; -.
DR PDBsum; 2RCB; -.
DR AlphaFoldDB; Q8VHN2; -.
DR SMR; Q8VHN2; -.
DR STRING; 10116.ENSRNOP00000017064; -.
DR BindingDB; Q8VHN2; -.
DR ChEMBL; CHEMBL1907608; -.
DR ChEMBL; CHEMBL2096669; -.
DR ChEMBL; CHEMBL4524129; -.
DR DrugCentral; Q8VHN2; -.
DR GlyGen; Q8VHN2; 6 sites.
DR PaxDb; Q8VHN2; -.
DR PRIDE; Q8VHN2; -.
DR GeneID; 170796; -.
DR KEGG; rno:170796; -.
DR UCSC; RGD:621705; rat.
DR CTD; 116444; -.
DR RGD; 621705; Grin3b.
DR eggNOG; KOG1053; Eukaryota.
DR InParanoid; Q8VHN2; -.
DR OrthoDB; 188544at2759; -.
DR PhylomeDB; Q8VHN2; -.
DR EvolutionaryTrace; Q8VHN2; -.
DR PRO; PR:Q8VHN2; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IDA:SynGO.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR GO; GO:0017146; C:NMDA selective glutamate receptor complex; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005261; F:cation channel activity; IDA:RGD.
DR GO; GO:0016594; F:glycine binding; IDA:RGD.
DR GO; GO:0004970; F:ionotropic glutamate receptor activity; IEA:InterPro.
DR GO; GO:0015276; F:ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0042165; F:neurotransmitter binding; IDA:RGD.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IDA:RGD.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IEA:GOC.
DR GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; IDA:RGD.
DR GO; GO:0051205; P:protein insertion into membrane; ISO:RGD.
DR GO; GO:0051924; P:regulation of calcium ion transport; ISO:RGD.
DR InterPro; IPR019594; Glu/Gly-bd.
DR InterPro; IPR001508; Iono_rcpt_met.
DR InterPro; IPR001320; Iontro_rcpt.
DR InterPro; IPR028082; Peripla_BP_I.
DR Pfam; PF00060; Lig_chan; 1.
DR Pfam; PF10613; Lig_chan-Glu_bd; 1.
DR PRINTS; PR00177; NMDARECEPTOR.
DR SMART; SM00918; Lig_chan-Glu_bd; 1.
DR SMART; SM00079; PBPe; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell membrane; Coiled coil; Glycoprotein;
KW Ion channel; Ion transport; Ligand-gated ion channel; Magnesium; Membrane;
KW Postsynaptic cell membrane; Receptor; Reference proteome; Signal; Synapse;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..1002
FT /note="Glutamate receptor ionotropic, NMDA 3B"
FT /id="PRO_0000011572"
FT TOPO_DOM 25..564
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 565..585
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 586..648
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 649..669
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 670..826
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 827..847
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 848..1002
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 882..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 951..984
FT /note="Involved in the trafficking and surface expression
FT of NMDARs"
FT /evidence="ECO:0000250"
FT COILED 944..985
FT /evidence="ECO:0000255"
FT COMPBIAS 892..910
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 451
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 786
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT STRAND 416..421
FT /evidence="ECO:0007829|PDB:2RCA"
FT TURN 425..427
FT /evidence="ECO:0007829|PDB:2RCA"
FT STRAND 428..432
FT /evidence="ECO:0007829|PDB:2RCA"
FT STRAND 440..446
FT /evidence="ECO:0007829|PDB:2RCA"
FT HELIX 453..465
FT /evidence="ECO:0007829|PDB:2RCA"
FT HELIX 470..472
FT /evidence="ECO:0007829|PDB:2RCA"
FT STRAND 473..478
FT /evidence="ECO:0007829|PDB:2RCA"
FT HELIX 479..491
FT /evidence="ECO:0007829|PDB:2RCA"
FT STRAND 494..499
FT /evidence="ECO:0007829|PDB:2RCA"
FT HELIX 515..521
FT /evidence="ECO:0007829|PDB:2RCA"
FT STRAND 526..528
FT /evidence="ECO:0007829|PDB:2RCA"
FT HELIX 536..539
FT /evidence="ECO:0007829|PDB:2RCA"
FT STRAND 542..544
FT /evidence="ECO:0007829|PDB:2RCA"
FT STRAND 548..558
FT /evidence="ECO:0007829|PDB:2RCA"
FT HELIX 683..686
FT /evidence="ECO:0007829|PDB:2RCA"
FT HELIX 701..709
FT /evidence="ECO:0007829|PDB:2RCA"
FT HELIX 711..717
FT /evidence="ECO:0007829|PDB:2RCA"
FT STRAND 722..724
FT /evidence="ECO:0007829|PDB:2RCA"
FT HELIX 725..733
FT /evidence="ECO:0007829|PDB:2RCA"
FT STRAND 734..736
FT /evidence="ECO:0007829|PDB:2RCA"
FT STRAND 740..745
FT /evidence="ECO:0007829|PDB:2RCA"
FT HELIX 746..755
FT /evidence="ECO:0007829|PDB:2RCA"
FT STRAND 761..773
FT /evidence="ECO:0007829|PDB:2RCA"
FT STRAND 776..778
FT /evidence="ECO:0007829|PDB:2RCA"
FT HELIX 784..796
FT /evidence="ECO:0007829|PDB:2RCA"
FT HELIX 799..807
FT /evidence="ECO:0007829|PDB:2RCA"
SQ SEQUENCE 1002 AA; 109158 MW; 4AC840EF97E0AB83 CRC64;
MESVRTLWLS VALALAVGSR VVRGHPQPCR VPTRAGASVR LAALLPRAPA ARARVLAALA
TPAPRLPHNL SLELVAVASP TRDPASLARG LCQVLAPPGV VASIAFPEAR PELRLLQFLA
AATETPVVSV LRREVRTALG APTPFHLQLD WASPLETILD VLVSLVRAHA WEDIALVLCR
VRDPGSLVTL WTNHASQAPK FVLDLSRLDS RNDSLRAGLA LLGALEGGGT PVPAAVLLGC
STARAHEVLE AAPPGPQWLL GTPLPAEALP TTGLPPGVLA LGETEQHSLE AVVHDMVELV
AQALSSMALV HPERALLPAV VNCDDLKTGG SEATGRTLAR FLGNTSFQGR TGAVWVTGSS
QVHVSRHFKV WSLRRDPLGA PAWATVGSWQ DGQLDFQPGA AALRVPSPSG TQARPKLRVV
TLVEHPFVFT RESDEDGQCP AGQLCLDPGT NDSARLDALF AALVNGSVPR TLRRCCYGYC
IDLLERLAED LAFDFELYIV GDGKYGALRD GRWTGLVGDL LAGRAHMAVT SFSINSARSQ
VVDFTSPFFS TSLGIMVRTR DTASPIGAFM WPLHWSMWVG VFAALHLTAL FLTLYEWRSP
YGLTPRGRNR GTVFSYSSAL NLCYAILFGR TVSSKTPKCP TGRFLMNLWA IFCLLVLSSY
TANLAAVMVG DKTFEELSGI HDPKLHHPSQ GFRFGTVWES SAEAYIKASF PEMHAHMRRH
SAPTTPHGVA MLTSDPPKLN AFIMDKSLLD YEVSIDADCK LLTVGKPFAI EGYGIGLPQN
SPLTSNLSEF ISRYKSSGFI DLLHDKWYKM VPCGKRVFAV TETLQMGVYH FSGLFVLLCL
GLGSALLTSL GEHVFYRLVL PRIRRGNKLQ YWLHTSQKIH RALNTGPPEG QQERAEQERS
GPKDELPATD GAGRWRRVRR AVERERRVRF LLEPGEAGGD RPWLCSNGPG LQAELRELEL
RIEAARERLR SALLRRGELR ALLGDGTRLR PLRLLHAAPA ES
